ID   CPD1_PHANO              Reviewed;         193 AA.
AC   Q0UME8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase;
DE            Short=CPDase;
DE            EC=3.1.4.37;
GN   Name=CPD1; ORFNames=SNOG_07066;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Involved in the metabolism of ADP-ribose 1',2'-cyclic
CC       phosphate which is produced as a consequence of tRNA splicing.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-
CC         phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CPD1 family.
CC       {ECO:0000305}.
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DR   EMBL; CH445334; EAT85717.1; -; Genomic_DNA.
DR   RefSeq; XP_001797420.1; XM_001797368.1.
DR   AlphaFoldDB; Q0UME8; -.
DR   SMR; Q0UME8; -.
DR   EnsemblFungi; SNOT_07066; SNOT_07066; SNOG_07066.
DR   GeneID; 5974310; -.
DR   KEGG; pno:SNOG_07066; -.
DR   eggNOG; ENOG502S8HR; Eukaryota.
DR   HOGENOM; CLU_108991_1_0_1; -.
DR   InParanoid; Q0UME8; -.
DR   OMA; WLDSIPW; -.
DR   OrthoDB; 1620665at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0009187; P:cyclic nucleotide metabolic process; IBA:GO_Central.
DR   InterPro; IPR012386; Cyclic-nucl_3Pdiesterase.
DR   InterPro; IPR009097; Cyclic_Pdiesterase.
DR   PANTHER; PTHR28141; PTHR28141; 1.
DR   Pfam; PF07823; CPDase; 1.
DR   SUPFAM; SSF55144; SSF55144; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus; Hydrolase; Reference proteome.
FT   CHAIN           1..193
FT                   /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT                   /id="PRO_0000280680"
FT   ACT_SITE        40
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        129
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  21405 MW;  BAFF9C8086E1503D CRC64;
     MPGSSLWLLP PKSHRLNSIL PTLIDQTSSH FGSAHRFLPH VTITSEISPS THSPNPQAWL
     DSLEISSGDK IEVMFEKLAS EDVFFRKLYI KCHKTEGLKK LAVLCRREVE GFGEEREAAK
     WATESYNPHL SLLYHDCPSI DASGLAEIEK LAQSTGVNLN GQSDLGGWSG GRLVLVPTDK
     SIDQWSPIAE REL